Journal of Microbiology

Research Support, Non-U.S. Gov'ts

NOTE] Probing the ArcA Regulon in the Rumen Bacterium Mannheimia succiniciproducens by Genome-Wide Expression Profiling: Seulgi Yun , Jong Moon Shin , Oh-Cheol Kim , Young Ryul Jung , Doo-Byoung Oh , Sang Yup Lee , Ohsuk Kwon; J. Microbiol. 2012;50(4):665-672. Published online July 21, 2012; DOI: https://doi.org/10.1007/s12275-012-2007-7

Abstract: In this study, the putative target genes of the Arc two-component system of the rumen bacterium Mannheimia succiniciproducens were determined by analyzing the transcriptome of the ArcA overexpression strain and by the in silico scanning of the entire genome sequence with the position weight matrix of the ArcA binding sequence developed for Escherichia coli. The majority of 79 repressed genes were involved in energy metabolism and carbohydrate transport and metabolism, while the majority of 82 induced genes were involved in hypothetical or unknown functions. Our results suggest that the Arc system in M. succiniciproducens has a specific function that differs from that in E. coli.

NOTE] Evidence Against the Physiological Role of Acetyl Phosphate in the Phosphorylation of the ArcA Response Regulator in Escherichia coli: Xueqiao Liu , Gabriela R. Peña Sandoval , Barry L. Wanner , Won Seok Jung , Dimitris Georgellis , Ohsuk Kwon; J. Microbiol. 2009;47(5):657-662. Published online October 24, 2009; DOI: https://doi.org/10.1007/s12275-009-0087-9

Abstract: The Arc two-component signal transduction system of Escherichia coli comprises the ArcB sensor kinase and the ArcA response regulator. Under anoxic growth conditions, ArcB autophosphorylates and transphosphorylates ArcA, which, in turn, represses or activates its target operons. ArcA has been shown to be able to autophosphorylate in vitro at the expense of acetyl-P. Here, the in vivo effect of acetyl phosphate on the redox signal transduction by the Arc system was assessed. Our results indicate that acetyl phosphate can modulate the expression of ArcA-P target genes only in the absence of ArcB. Therefore, the acetyl phosphate dependent ArcA phosphorylation route does not seem to play a significant role under physiological conditions.

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